MGD LECTURE 2.1 ENZYME ACTIVITY: KINETICS AND INHIBITION Flashcards

1
Q

Whats is an enzyme?

A

Biological catalyst which increases rate of reaction by lowering activation energy

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2
Q

What do enzymes facilitate the formation of?

A

The transition state, also known as a high energy intermediate

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3
Q

What are active sites?

A

Usually clefts or crevices which exclude water. Complementary shape to that of substrate.

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4
Q

What is induced fit model?

A

Binding of substrate induces changes in conformation of enzyme

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5
Q

How big is an enzymes active site?

A

> 100 amino acids

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6
Q

How are substrates bound to enzymes?

A

By all types of non-covalent bonds

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7
Q

What is Vo?

A

initial rate of reaction

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8
Q

how does an increase of temperature affect enzyme function?

A

increases number of molecules with activation energy

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9
Q

How does an increase in concentration of substrate affect enzyme function?

A

increases chance of molecular collisions

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10
Q

What is KM?

A

substrate conc which gives half maximal velocity

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11
Q

What is Vmax?

A

Maximal rate when all enzyme active sites are saturated with substrate

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12
Q

What does the michaelis menten equation predict?

A

A plot of Vo versus S will be a rectangular hyperbole

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13
Q

What does it mean if an enzyme has a low km?

A

high affinity for its substrate

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14
Q

What does the lineweaver burk plot allow for?

A

Easy estimation of km (gradient = km/vmax) and vmax (y intercept is 1/vmax)

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15
Q

What is an enzyme inhibitor?

A

A molecule that slows down or prevents an enzyme reaction.

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16
Q

what bonds are formed in irreversible enzyme reactions?

A

covalent

17
Q

What does a competitive inhibitor effect?

A

km, not vmax (more inhibitor, higher km)

18
Q

what does a non competitive inhibitor effect?

A

Vmax, but not KM (more inhibitor, vmax decreases)